MAG is a member of the SIGLEC family of proteins and is a functional ligand of the NOGO-66 receptor, NgR.

[9] Uncleaved MAG is a complete transmembrane form, which acts as a signaling and adhesion molecule.

MAG-oligosaccharide complex structures and biophysical assays show how MAG engages axonal gangliosides at domain Ig1.

[18] MAG binds with high affinity to NgR, suggesting that it is equally as responsible for inhibition of axon regeneration as Nogo.

The activation of the rho kinase pathway leads to the phosphorylation of proteins which inhibit neurite outgrowth.